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GLUTATHIONE TRANSFERASES

Annual Review of Pharmacology and Toxicology, 2005
▪ Abstract  This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β ...
Hayes, John D.   +2 more
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Measurement of Glutathione Transferases

Current Protocols in Toxicology, 2002
AbstractThere are multiple glutathione transferase genes, the proteins for which have different substrate specificities. The various genes are differentially expressed such that species and organs and tissues differ qualitatively and quantitatively for cytosolic and membrane‐bound forms. This unit provides protocols for analysis of transferase activity
B, Mannervik, P, Jemth
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Insect glutathione transferases

Drug Metabolism Reviews, 2011
This article is an overview of the current knowledge of insect glutathione transferases. Three major topics are discussed: the glutathione transferase contributions to insecticide resistance, the polymorphic nature of the insect glutathione transferase superfamily, and a summary of the current structure-function studies on insect glutathione ...
Albert J, Ketterman   +2 more
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Glutathione Transferases and Cancer

Critical Reviews in Biochemistry and Molecular Biology, 1992
The glutathione transferases, a family of multifunctional proteins, catalyze the glutathione conjugation reaction with electrophilic compounds biotransformed from xenobiotics, including carcinogens. In preneoplastic cells as well as neoplastic cells, specific molecular forms of glutathione transferase are known to be expressed and have been known to ...
S, Tsuchida, K, Sato
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Glutathione S-Transferases

1996
Glutathione (GSH), the most ubiquitous and abundant nonprotein thiol, is essential in numerous detoxification reactions and is therefore considered a chemoprotectant. In the human, levels of GSH range from 30μM in plasma to 3mM in kidney proximal tubules; tumors of various organs can contain up to 10mM GSH [1].
A, Raha, K D, Tew
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Glutathione Transferases and Carcinogenesis

1986
Carcinogenesis has been regarded as being divisible into at least 3 major phases: (a) initiation, a largely irreversible process which has been compared to mutation; (b) promotion, a process during which cells undergo phenotypic changes, some of which are referred to as preneoplastic, and a proportion of which attain autonomy when they can be regarded ...
B, Ketterer   +4 more
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Mosquito Glutathione Transferases

2005
The glutathione transferases (glutathione S-transferases, GSTs) are a diverse family of enzymes involved in a wide range of biological processes, many of which involve the conjugation of the tripeptide glutathione to an electrophilic substrate. Relatively little is known about the endogenous substrates of mosquito GSTs, and most studies have focused on
Hilary, Ranson, Janet, Hemingway
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Glutathione transferases and neurodegenerative diseases

Neurochemistry International, 2015
There is substantial agreement that the unbalance between oxidant and antioxidant species may affect the onset and/or the course of a number of common diseases including Parkinson's and Alzheimer's diseases. Many studies suggest a crucial role for oxidative stress in the first phase of aging, or in the pathogenesis of various diseases including ...
MAZZETTI, ANNA PAOLA   +3 more
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Human Glutathione S-Transferases

Seminars in Liver Disease, 1998
Human glutathione S-transferases (GSTs) are a functionally diverse family of soluble enzymes of detoxification that use reduced glutathione (GSH) in conjugation and reduction reactions. Toxic electrophiles, including a variety of carcinogens, are substrates for the GSTs and after conjugation or reduction they are more easily excreted into bile or urine.
R, Whalen, T D, Boyer
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The glutathione peroxidase activity of glutathione S-transferases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
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